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Article

Structure of the Cyclin T binding domain of Hexim1 and molecular basis for its recognition of P-TEFb.

Proceedings of the National Academy of Sciences of the United States of America - 4 Sept 2007

Dames Sonja A, Schönichen André, Schulte Antje, Barboric Matjaz, Peterlin B Matija, Grzesiek Stephan, Geyer Matthias

Abstract excerpt

Hexim1 is a cellular protein that associates with the positive transcription elongation factor b (P-TEFb) to regulate RNA polymerase II elongation of nascent mRNA transcripts. It directly binds to Cyclin T1 of P-TEFb and inhibits the kinase activity of Cdk9, leading to an arrest of transcription elongation. Here, we report the solution structure of the Cyclin T binding domain (TBD) of Hexim1 that forms a parallel...

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Identifiers

PMID: 17724342
DOI: 10.1073/pnas.0701848104
PMCID: PMC1955226

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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